ID A0A2H3DDF2_ARMGA Unreviewed; 937 AA.
AC A0A2H3DDF2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Fanconi-associated nuclease {ECO:0000256|RuleBase:RU365033};
DE EC=3.1.4.1 {ECO:0000256|RuleBase:RU365033};
GN ORFNames=ARMGADRAFT_966786 {ECO:0000313|EMBL:PBK93269.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK93269.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of
CC DNA and cleaves DNA successively at every third nucleotide, allowing to
CC excise an ICL from one strand through flanking incisions.
CC {ECO:0000256|RuleBase:RU365033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000256|ARBA:ARBA00000983,
CC ECO:0000256|RuleBase:RU365033};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU365033};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU365033};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365033}.
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000256|ARBA:ARBA00005533,
CC ECO:0000256|RuleBase:RU365033}.
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DR EMBL; KZ293657; PBK93269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3DDF2; -.
DR STRING; 47427.A0A2H3DDF2; -.
DR InParanoid; A0A2H3DDF2; -.
DR OMA; ECRVESM; -.
DR OrthoDB; 38749at2759; -.
DR Proteomes; UP000217790; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR CDD; cd22326; FAN1-like; 1.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR049132; FAN1-like_euk.
DR InterPro; IPR049126; FAN1-like_TPR.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR PANTHER; PTHR15749:SF4; FANCONI-ASSOCIATED NUCLEASE 1; 1.
DR Pfam; PF21170; FAN1_TPR; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|RuleBase:RU365033};
KW DNA repair {ECO:0000256|RuleBase:RU365033};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365033};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU365033};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU365033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365033};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU365033};
KW Nucleus {ECO:0000256|RuleBase:RU365033};
KW Reference proteome {ECO:0000313|Proteomes:UP000217790}.
FT DOMAIN 728..843
FT /note="VRR-NUC"
FT /evidence="ECO:0000259|SMART:SM00990"
FT REGION 151..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..44
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 878..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 108206 MW; 48424E4C91B99C7F CRC64;
MRPVNENDAI NLIFGGGLEV EEELSDIEDE IEELDATQRK EKSERPSTYV RVMEDMINEV
DSYESHLLSE DEWCLIRLFG KEMKYHARYL LVRLLCRKQN RWHSFNALHR YTSEIGEDGI
RQAITDLAAA LEPSEEAEVK VEEPEIIDLT LDEEEKEDRK PVAGSSRLAT PPQTQSKDGA
FEAVIENLDL SYFCKDESTM TLREILETLP ADQVRALAKE ARVSPKGTKK ENFVNALMKY
SSTQASLPFQ SPKKIKSRQA ERYDDGYRQT VLCFAVPCKE TQEQRLKEMA LNRLGKCIRL
NYDFFRLVRR FSIIFYRSMH LPADIFLPSL LSEFKKRIYP KYNATRTGQI WESREAFLQY
EEALHFEAEL EAILESEEKV LRASITPKRG TATPGKTPRP VKADDDEAMD DVDDGDWLSP
QQMVAKAVRE KVMNTILPRW RLCVAVKRAV KKEAHGEDPR PGLDRFEPGY IYTRMVEKYA
RALGQLKEYE VEVETLDELL GQRFWRRGKR GSWYDRRALV EITYLSKVEG KKSKSRPKLK
IAMEHLKDAL RDEDTHLICR PGLFRRLQKV ETALRVPEEQ RSQCEGELKK PEEVKVQAER
IKRSSTSLQL DQFGRPKGKE NGAPGSSRTK DGGMTPSWTG KSLWRGERNE EVNVETRTLQ
AYAEQGYKGF HSETRILTTI FGLLFWDIIF ADVPGAFETK FQTAPLDIAE DSFYYARKEL
IQARLREIED GKAAEIMERH DRTYRPSKTW CVGVKWEYPK EDLLEIVQCF KGESLATICH
LFCEDYAGRS SGAPDLIVWK PEDRECKFVE VKGPGDRLQE NQKLWCDALQ RAGVEVQLCH
VVDVYGKAKR INKKRKKLEE ESFSGPEDDE DENIDEEAEY QPPQKHPDAE EEEHYPLAMS
QPRTTPTKWP TTKVEVVITS PSPMKKRRKL DVVSAGS
//
